An OPAA enzyme mutant with increased catalytic efficiency on the nerve agents sarin, soman, and GP.
Enzyme Microb Technol
; 112: 65-71, 2018 May.
Article
em En
| MEDLINE
| ID: mdl-29499783
ABSTRACT
The wild-type OPAA enzyme has relatively high levels of catalytic activity against several organophosphate G-type nerve agents. A series of mutants containing replacement amino acids at the OPAA Y212, V342, and I215 sites showed several fold enhanced catalytic efficiency on sarin, soman, and GP. One mutant, Y212F/V342L, showed enhanced stereospecificity on sarin and that enzyme along with a phosphotriesterase mutant, GWT, which had the opposite stereospecificity, were used to generate enriched preparations of each sarin enantiomer. Inhibition of acetylcholinesterase by the respective enantioenriched sarin solutions subsequently provided identification of the sarin enantiomers as separated by normal phase enantioselective liquid chromatography coupled with atmospheric pressure chemical ionization-mass spectrometry.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Arildialquilfosfatase
/
Agentes Neurotóxicos
Idioma:
En
Revista:
Enzyme Microb Technol
Ano de publicação:
2018
Tipo de documento:
Article